Bacterial Proteases and Virulence
Abstract
Bacterial pathogens rely on proteolysis for variety of purposes during the infection process. In the cytosol, the main proteolytic players are the conserved Clp and Lon proteases that directly contribute to virulence through the timely degradation of virulence regulators and indirectly by providing tolerance to adverse conditions such as those experienced in the host. In the membrane, HtrA performs similar functions whereas the extracellular proteases, in close contact with host components, pave the way for spreading infections by degrading host matrix components or interfering with host cell signalling to short-circuit host cell processes. Common to both intra- and extracellular proteases is the tight control of their proteolytic activities. In general, substrate recognition by the intracellular proteases is highly selective which is, in part, attributed to the chaperone activity associated with the proteases either encoded within the same polypeptide or on separate subunits. In contrast, substrate recognition by extracellular proteases is less selective and therefore these enzymes are generally expressed as zymogens to prevent premature proteolytic activity that would be detrimental to the cell. These extracellular proteases are activated in complex cascades involving auto-processing and proteolytic maturation. Thus, proteolysis has been adopted by bacterial pathogens at multiple levels to ensure the success of the pathogen in contact with the human host.
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Pathogen-dependent extracellular proteases facilitate host invasion by degrading host extracellular matrix components or by interfering with host cell and immune signaling.
“In contrast, pathogen-dependent extracellular proteases facilitate host invasion by degrading host extracellular matrix components or by interfering with host cell and immune signaling, as we discuss in the next section.11”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [11]
Intracellular and membrane proteases such as Clp, Lon or HtrA contribute to virulence through the timely degradation of virulence regulators and indirectly by providing tolerance to adverse conditions in the host.
“Intracellular and membrane proteases such as Clp, Lon or HtrA contribute to virulence through the timely degradation of virulence regulators and indirectly by providing tolerance to adverse conditions in the host.”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [11]
Cites
Autoinduction and signal transduction in the regulation of staphylococcal virulence
Novick, R. P. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03526.x · Cited by 1,271 · see citing works
Immune evasion by staphylococci
Foster, T. J. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1289 · Cited by 1,214 · see citing works
Streptococcal Infections of Skin and Soft Tissues
Bisno, A. L., & Stevens, D. L. (1996) · New England Journal of Medicine · doi:10.1056/nejm199601253340407 · Cited by 990 · see citing works
Surface protein adhesins of Staphylococcus aureus
Foster, T. J., & Höök, M. (1998) · Trends in Microbiology · doi:10.1016/s0966-842x(98)01400-0 · Cited by 985 · see citing works
agr-Mediated Dispersal of Staphylococcus aureus Biofilms
Boles, B. R., & Horswill, A. R. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000052 · Cited by 972 · see citing works
Otto, M. J. (2008) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-75418-3_10 · Cited by 903 · see citing works
A Temperature-Dependent Switch from Chaperone to Protease in a Widely Conserved Heat Shock Protein
Spiess, C., Beil, A., & Ehrmann, M. (1999) · Cell · doi:10.1016/s0092-8674(00)80743-6 · Cited by 768 · see citing works
The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis
Wang, J., Hartling, J. A., & Flanagan, J. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80431-6 · Cited by 591 · see citing works
Phagocytosis and innate immunity
Greenberg, S., & Grinstein, S. (2002) · Current Opinion in Immunology · doi:10.1016/s0952-7915(01)00309-0 · Cited by 581 · see citing works
Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus -Derived Proteinases
Sieprawska‐Lupa, M., Mydel, P. M., Krawczyk, K., Wójcik, K., Puklo, M., Lupa, B., Suder, P., Silberring, J., Reed, M. S., Pohl, J., et al. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.12.4673-4679.2004 · Cited by 552 · see citing works
The alternative sigma factor katF (rpoS) regulates Salmonella virulence.
Fang, F. C., Libby, S. J., Buchmeier, N. A., Loewen, P. C., Switala, J., Harwood, J. I., & Guiney, D. G. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.11978 · Cited by 516 · see citing works
Dysregulation of bacterial proteolytic machinery by a new class of antibiotics
Brötz-Oesterhelt, H., Beyer, D., Kroll, H.-P., Endermann, R., Ladel, C., Schroeder, W., Hinzen, B., Raddatz, S., Paulsen, H., Henninger, K., et al. (2005) · Nature Medicine · doi:10.1038/nm1306 · Cited by 505 · see citing works
Bacterial flagellins: mediators of pathogenicity and host immune responses in mucosa
Ramos, H. C., Rumbo, M., & Sirard, J. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.09.002 · Cited by 485 · see citing works
HTRA proteases: regulated proteolysis in protein quality control
Clausen, T., Kaiser, M., Huber, R., & Ehrmann, M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3065 · Cited by 479 · see citing works
IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G
von Pawel‐Rammingen, U., Johansson, B. P., & Björck, L. (2002) · The EMBO Journal · doi:10.1093/emboj/21.7.1607 · Cited by 475 · see citing works
Structure and function of the plasminogen/plasmin system
Ploplis, V. A., & Castellino, F. (2005) · Thrombosis and Haemostasis · doi:10.1160/th04-12-0842 · Cited by 460 · see citing works
Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL‐37
Schmidtchen, A., Frick, I.-M., Andersson, E., Tapper, H., & Björck, L. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03146.x · Cited by 440 · see citing works
Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
Krojer, T. J., Garrido-Franco, M., Huber, R., Ehrmann, M., & Clausen, T. (2002) · Nature · doi:10.1038/416455a · Cited by 403 · see citing works
Structural basis for the regulated protease and chaperone function of DegP
Krojer, T. J., Sawa-Makarska, J. Z., Schäfer, E., Saibil, H. R., Ehrmann, M., & Clausen, T. (2008) · Nature · doi:10.1038/nature07004 · Cited by 368 · see citing works
Collin, M., & Olsén, A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.12.3046 · Cited by 367 · see citing works
Lipińska, B., Fayet, O., Baird, L. M., & Georgopoulos, C. P. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.3.1574-1584.1989 · Cited by 342 · see citing works
Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence
Frees, D., Qazi, S. N. A., Hill, P. J., & Ingmer, H. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03524.x · Cited by 328 · see citing works
Self-citationFrees, D., Chastanet, A., Qazi, S. N. A., Sørensen, K., Hill, P. J., Msadek, T., & Ingmer, H. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04368.x · Cited by 327 · see citing works
Self-citationLipińska, B., Żylicz, M., & Georgopoulos, C. P. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.4.1791-1797.1990 · Cited by 325 · see citing works
entry into host cells: the work in concert of type III secreted effector proteins
Zhou, D., & Galán, J. E. (2001) · Microbes and Infection · doi:10.1016/s1286-4579(01)01489-7 · Cited by 325 · see citing works
Guina, T., Yi, E. C., Wang, H., Hackett, M., & Miller, S. I. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.14.4077-4086.2000 · Cited by 322 · see citing works
Hoy, B., Löwer, M., Weydig, C., Carra, G., Tegtmeyer, N., Geppert, T., Schröder, P., Sewald, N., Backert, S., Schneider, G., et al. (2010) · The EMBO Reports · doi:10.1038/embor.2010.114 · Cited by 295 · see citing works
Clp P represents a unique family of serine proteases.
Maurizi, M. R., Clark, W. P., Kim, S. H., & Gottesman, S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38379-6 · Cited by 288 · see citing works
Frees, D., Savijoki, K., Varmanen, P., & Ingmer, H. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05598.x · Cited by 288 · see citing works
Self-citationStaphylococcus aureus genetic loci impacting growth and survival in multiple infection environments
Coulter, S. N., Schwan, W. R., Ng, E. Y. W., Langhorne, M. H., Ritchie, H., Westbrock-Wadman, S., HUFNAGLE, W. O., Folger, K. R., Bayer, A. S., & Stover, C. K. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.01075.x · Cited by 284 · see citing works
The role and regulation of the extracellular proteases of Staphylococcus aureus
Shaw, L. N., Golonka, E., Potempa, J., & Foster, S. J. (2003) · Microbiology · doi:10.1099/mic.0.26634-0 · Cited by 281 · see citing works
The role of a stress‐response protein in Salmonella typhimurium virulence
Johnson, K. S., Charles, I. G., Gordon Dougan, B., Pickard, D., Gaora, P. Ó., Costa, G., Ali, T., Miller, I. A., & Hormaeche, C. E. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb02122.x · Cited by 273 · see citing works
Gaillot, O., Pellegrini, E., Bregenholt, S., Nair, S., & Berche, P. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01773.x · Cited by 269 · see citing works
Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase.
Kim, Y.-I., Levchenko, I. V., Fraczkowska, K., Woodruff, R. V., Sauer, R. T., & Baker, T. A. (2001) · Nature Structural Biology · doi:10.1038/84967 · Cited by 263 · see citing works
Salmonella typhimurium loci involved in survival within macrophages
Bäumler, A. J., Kusters, J. G., Stojiljković, I., & Heffron, F. (1994) · Infection and Immunity · doi:10.1128/iai.62.5.1623-1630.1994 · Cited by 241 · see citing works
Humphreys, S., Stevenson, A. W., Bacon, A. K., Weinhardt, A. B., & Roberts, M. (1999) · Infection and Immunity · doi:10.1128/.67.4.1560-1568.1999 · Cited by 236 · see citing works
Bever, R., & Iglewski, B. H. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.9.4309-4314.1988 · Cited by 232 · see citing works
Recognition of misfolded proteins by Lon, a AAA + proteasePreprint
Gur, E., & Sauer, R. T. (2008) · Genes & Development · doi:10.1101/gad.1670908 · Cited by 232 · see citing works
Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism
Lee, B., Park, E. Y., Lee, K.-E., Jeon, H., Sung, K. H., Paulsen, H., Rübsamen‐Schaeff, H., Brötz‐Oesterhelt, H., & Song, H. K. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1787 · Cited by 230 · see citing works
Lucas, R. L., Lostroh, P., Dirusso, C., Spector, M. P., Wanner, B. L., & Lee, C. A. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.7.1872-1882.2000 · Cited by 225 · see citing works
The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease
Kirstein, J., Hoffmann, A., Lilie, H., Schmidt, R., Rübsamen‐Waigmann, H., Brötz‐Oesterhelt, H., Mogk, A., & Turgay, K. (2009) · EMBO Molecular Medicine · doi:10.1002/emmm.200900002 · Cited by 222 · see citing works
Michel, A., Agerer, F., Hauck, C. R., Herrmann, M., Ullrich, J., Hacker, J. H., & Ohlsen, K. (2006) · Journal of Bacteriology · doi:10.1128/jb.00074-06 · Cited by 214 · see citing works
Proteome Analysis of Secreted Proteins of the Gastric Pathogen Helicobacter pylori
Bumann, D., Aksu, S., Wendland, M., Janek, K., Zimny-Arndt, U., Sabarth, N., Meyer, T. F., & Jungblut, P. R. (2002) · Infection and Immunity · doi:10.1128/iai.70.7.3396-3403.2002 · Cited by 209 · see citing works
Böttcher, T., & Sieber, S. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8051365 · Cited by 207 · see citing works
Biological roles of the Lon ATP-dependent protease
Tsilibaris, V., Maenhaut-Michel, G., & Melderen, L. V. (2006) · Research in Microbiology · doi:10.1016/j.resmic.2006.05.004 · Cited by 207 · see citing works
Effect of SpeB and EndoS from Streptococcus pyogenes on Human Immunoglobulins
Collin, M., & Olsén, A. (2001) · Infection and Immunity · doi:10.1128/iai.69.11.7187-7189.2001 · Cited by 205 · see citing works
Antibiotic acyldepsipeptides activate ClpP peptidase to degrade the cell division protein FtsZ
Saß, P., Josten, M., Famulla, K., Schiffer, G., Sahl, H., Hamoen, L. W., & Brötz‐Oesterhelt, H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110385108 · Cited by 197 · see citing works
Schmitt, E. K., Riwanto, M., Sambandamurthy, V. K., Roggo, S. P., Miault, C., Zwingelstein, C., Krastel, P., Noble, C. G., Beer, D., Rao, S. P. S., et al. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201101740 · Cited by 196 · see citing works
The IL-8 Protease SpyCEP/ScpC of Group A Streptococcus Promotes Resistance to Neutrophil Killing
Zinkernagel, A. S., Timmer, A. M., Pence, M. A., Locke, J. B., Buchanan, J. T., Turner, C. E., Mishalian, I., Sriskandan, S., Hanski, E., & Nizet, V. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.07.002 · Cited by 184 · see citing works
Modification of the Staphylococcus aureus fibronectin binding phenotype by V8 protease
Mcgavin, M. J., Zahradka, C., Rice, K. C., & Scott, J. E. (1997) · Infection and Immunity · doi:10.1128/iai.65.7.2621-2628.1997 · Cited by 168 · see citing works
Rice, K. C., Peralta, R., Bast, D. J., de Azavedo, J., & Mcgavin, M. J. (2001) · Infection and Immunity · doi:10.1128/iai.69.1.159-169.2001 · Cited by 167 · see citing works
Li, D. H. S., Chung, Y. S., Gloyd, M., Ebenezer, J., Ghirlando, R., Wright, G. D., Cheng, Y., Maurizi, M. R., Guarné, A., & Ortega, J. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.07.008 · Cited by 166 · see citing works
Hidalgo‐Grass, C., Mishalian, I., Dan‐Goor, M., Belotserkovsky, I., Eran, Y., Nizet, V., Peled, A., & Hanski, E. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601327 · Cited by 157 · see citing works
Karlsson, A., Saravia‐Otten, P., Tegmark, K., Morfeldt, E., & Arvidson, S. (2001) · Infection and Immunity · doi:10.1128/iai.69.8.4742-4748.2001 · Cited by 157 · see citing works
McAleese, F., Walsh, E. J., Sieprawska, M., Potempa, J., & Foster, T. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102389200 · Cited by 153 · see citing works
Robertson, G. T., Ng, W., Foley, J., Gilmour, R., & Winkler, M. E. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.13.3508-3520.2002 · Cited by 150 · see citing works
Specific cleavage of human type III and IV collagens by Pseudomonas aeruginosa elastase
Heck, L. W., Morihara, K., McRae, W. B., & Miller, E. J. (1986) · Infection and Immunity · doi:10.1128/iai.51.1.115-118.1986 · Cited by 146 · see citing works
Jackson, M. W., Silva‐Herzog, E., & Plano, G. V. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04353.x · Cited by 144 · see citing works
Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins
Krojer, T. J., Pangerl, K., Kurt, J., Sawa-Makarska, J. Z., Stingl, C., Mechtler, K., Huber, R., Ehrmann, M., & Clausen, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803392105 · Cited by 142 · see citing works
How do neutrophils and pathogens interact?
Mayer‐Scholl, A. (2004) · Current Opinion in Microbiology · doi:10.1016/j.mib.2003.12.004 · Cited by 142 · see citing works
Extracellular proteases inhibit protein-dependent biofilm formation in Staphylococcus aureus
Martí, M., Trotonda, M. P., Tormo‐Más, M. Á., Vergara-Irigaray, M., Cheung, A. L., Lasa, Í., & Penadés, J. R. (2009) · Microbes and Infection · doi:10.1016/j.micinf.2009.10.005 · Cited by 140 · see citing works
Induction of group A Streptococcus virulence by a human antimicrobial peptide
Gryllos, I., Tran-Winkler, H. J., Cheng, M., Chung, H., Bolcome, R. E., Lu, W., Lehrer, R. I., & Wessels, M. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803815105 · Cited by 139 · see citing works
Molecular Characterization of a NovelStaphylococcus aureusSerine Protease Operon
Reed, S. B., Wesson, C. A., Liou, L. E., Trumble, W. R., Schlievert, P. M., Bohach, G. A., & Bayles, K. W. (2001) · Infection and Immunity · doi:10.1128/iai.69.3.1521-1527.2001 · Cited by 136 · see citing works
Chan, P. F., & Foster, S. J. (1998) · Microbiology · doi:10.1099/00221287-144-9-2469 · Cited by 133 · see citing works
EndoS and SpeB fromStreptococcus pyogenesInhibit Immunoglobulin-Mediated Opsonophagocytosis
Collin, M., Svensson, M. D., Sjöholm, A. G., Jensenius, J. C., Sjöbring, U., & Olsén, A. (2002) · Infection and Immunity · doi:10.1128/iai.70.12.6646-6651.2002 · Cited by 132 · see citing works
Takaya, A., Suzuki, M., Matsui, H., Tomoyasu, T., Sashinami, H., Nakane, A., & Yamamoto, T. (2003) · Infection and Immunity · doi:10.1128/iai.71.2.690-696.2003 · Cited by 131 · see citing works
Ruı́z-Pérez, F., Henderson, I. R., Leyton, D. L., Rossiter, A. E., Zhang, Y., & Nataro, J. P. (2009) · Journal of Bacteriology · doi:10.1128/jb.00754-09 · Cited by 129 · see citing works
Role of metalloprotease in activation of the precursor of staphylococcal protease
Drapeau, G. R. (1978) · Journal of Bacteriology · doi:10.1128/jb.136.2.607-613.1978 · Cited by 128 · see citing works
Schechter, L. M., & Lee, C. A. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02462.x · Cited by 128 · see citing works
Woo, K. M., Chung, W. J., Ha, D. B. D., Goldberg, A. L., & Chung, C. H. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94145-1 · Cited by 123 · see citing works
Purdy, G. E., Fisher, C. R., & Payne, S. M. (2007) · Journal of Bacteriology · doi:10.1128/jb.00483-07 · Cited by 123 · see citing works
Takaya, A., Tomoyasu, T., Tokumitsu, A., Morioka, M., & Yamamoto, T. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.1.224-232.2002 · Cited by 123 · see citing works
Degradation of elastin by a cysteine proteinase from Staphylococcus aureus.
Potempa, J., Dubin, A., Korzus, G., & Travis, J. W. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69118-5 · Cited by 119 · see citing works
Self‐compartmentalized bacterial proteases and pathogenesis
Butler, S. M., Festa, R. A., Pearce, M. J., & Darwin, K. H. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05128.x · Cited by 119 · see citing works
Elzer, P. H., Phillips, R. W., Kovach, M. E., Peterson, K. M., & Roop, R. M. (1994) · Infection and Immunity · doi:10.1128/iai.62.10.4135-4139.1994 · Cited by 117 · see citing works
Effects of DksA and ClpP protease on sigma S production and virulence in Salmonella typhimurium
Webb, C. C., Moreno, M. S., Wilmes-Riesenberg, M. R., Curtiss, R., & Foster, J. W. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01581.x · Cited by 116 · see citing works
Tomoyasu, T., Takaya, A., Isogai, E., & Yamamoto, T. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03437.x · Cited by 111 · see citing works
IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of
VONPAWELRAMMINGEN, U., & Björck, L. (2003) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(03)00003-1 · Cited by 109 · see citing works
Kwon, H., Ogunniyi, A. D., Choi, M., Pyo, S., Rhee, D., & Paton, J. C. (2004) · Infection and Immunity · doi:10.1128/iai.72.10.5646-5653.2004 · Cited by 107 · see citing works
Identification of Campylobacter jejuni Genes Involved in Its Interaction with Epithelial Cells
Novik, V., Hofreuter, D., & Galán, J. E. (2010) · Infection and Immunity · doi:10.1128/iai.00109-10 · Cited by 107 · see citing works
Rosch, J. W., & Caparon, M. G. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04887.x · Cited by 105 · see citing works
Tomoyasu, T., Ohkishi, T., Ukyo, Y., Tokumitsu, A., Takaya, A., Suzuki, M., Sekiya, K., Matsui, H., Kutsukake, K., & Yamamoto, T. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.3.645-653.2002 · Cited by 105 · see citing works
Boddicker, J. D., & Jones, B. D. (2004) · Infection and Immunity · doi:10.1128/iai.72.4.2002-2013.2004 · Cited by 103 · see citing works
Lyon, W. R., & Caparon, M. G. (2004) · Infection and Immunity · doi:10.1128/iai.72.3.1618-1625.2004 · Cited by 102 · see citing works
Iyoda, S., & Watanabe, H. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.12.4086-4094.2005 · Cited by 102 · see citing works
Massimi, I., Park, E., Rice, K. C., Müller‐Esterl, W., Sauder, D. N., & Mcgavin, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207162200 · Cited by 101 · see citing works
Intrinsic Thermal Sensing Controls Proteolysis of Yersinia Virulence Regulator RovA
Herbst, K., Bujara, M., Heroven, A. K., Opitz, W., Weichert, M., Zimmermann, A., & Dersch, P. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000435 · Cited by 101 · see citing works
ClpC ATPase Is Required for Cell Adhesion and Invasion of Listeria monocytogenes
Nair, S., Milohanic, E., & Berche, P. (2000) · Infection and Immunity · doi:10.1128/iai.68.12.7061-7068.2000 · Cited by 101 · see citing works
Proteolysis and its regulation at the surface of Streptococcus pyogenes
Rasmussen, M., & Björck, L. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02766.x · Cited by 98 · see citing works
Brøndsted, L., Andersen, M. T., Parker, M., Jørgensen, K., & Ingmer, H. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.6.3205-3212.2005 · Cited by 98 · see citing works
Self-citationRole of HtrA in Surface Protein Expression and Biofilm Formation by Streptococcus mutans
Biswas, S., & Biswas, I. (2005) · Infection and Immunity · doi:10.1128/iai.73.10.6923-6934.2005 · Cited by 98 · see citing works
Takaya, A., Kubota, Y., Isogai, E., & Yamamoto, T. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04425.x · Cited by 94 · see citing works
Rotanova, T. V., Botos, I., Melnikov, E. E., Rasulova, F. S., Gustchina, A., Maurizi, M. R., & Wlodawer, A. (2006) · Protein Science · doi:10.1110/ps.052069306 · Cited by 93 · see citing works
Medicinal Chemistry Optimization of Acyldepsipeptides of the Enopeptin Class Antibiotics
Hinzen, B., Raddatz, S., Paulsen, H., Lampe, T. F. J., Schumacher, A., Häbich, D., Hellwig, V., Benet‐Buchholz, J., Endermann, R., Labischinski, H., et al. (2006) · ChemMedChem · doi:10.1002/cmdc.200600055 · Cited by 92 · see citing works
Champion, O. L., Karlyshev, A. V., Senior, N. J., Woodward, M. J., Ragione, R. M. L., Howard, S. L., Wren, B. W., & Titball, R. W. (2010) · The Journal of Infectious Diseases · doi:10.1086/650494 · Cited by 91 · see citing works
Sumby, P., Zhang, S., Whitney, A. R., Falugi, F., Grandi, G., Graviss, E. A., DeLeo, F. R., & Musser, J. M. (2008) · Infection and Immunity · doi:10.1128/iai.01354-07 · Cited by 91 · see citing works
Cha, S., An, Y. J., Lee, C.-R., Lee, H. S., Kim, Y., Kim, S.-J., Kwon, K. K., Donatis, G. M. D., Lee, J., Maurizi, M. R., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.226 · Cited by 89 · see citing works
Chaussee, M. S., Phillips, E., & Ferretti, J. J. (1997) · Infection and Immunity · doi:10.1128/iai.65.5.1956-1959.1997 · Cited by 88 · see citing works
Ohbayashi, T., Irie, A., Murakami, Y., Nowak, M., Potempa, J., Nishimura, Y., Shinohara, M., & Imamura, T. (2010) · Microbiology · doi:10.1099/mic.0.044503-0 · Cited by 88 · see citing works
Yamamoto, T., Sashinami, H., Takaya, A., Tomoyasu, T., Matsui, H., Kikuchi, Y., Hanawa, T., Kamiya, S., & Nakane, A. (2001) · Infection and Immunity · doi:10.1128/iai.69.5.3164-3174.2001 · Cited by 85 · see citing works
Löwer, M., Weydig, C., Metzler, D., Reuter, A., Starzinski‐Powitz, A., Weßler, S., & Schneider, G. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003510 · Cited by 84 · see citing works
Listeria monocytogenes10403S HtrA Is Necessary for Resistance to Cellular Stress and Virulence
Wilson, R. L., Brown, L. L., Kirkwood-Watts, D. L., Warren, T. K., Lund, S. A., King, D. S., Jones, K. F., & Hruby, D. E. (2005) · Infection and Immunity · doi:10.1128/iai.74.1.765-768.2006 · Cited by 83 · see citing works
Lindsay, J. A., & Foster, S. J. (1999) · Molecular and General Genetics MGG · doi:10.1007/s004380051090 · Cited by 80 · see citing works
Bodelón, G., Marín, E., & Fernández, L. Á. (2009) · Journal of Bacteriology · doi:10.1128/jb.00458-09 · Cited by 79 · see citing works
Ibrahim, Y. M., Kerr, A. R., Silva, N. A., & Mitchell, T. J. (2005) · Infection and Immunity · doi:10.1128/iai.73.2.730-740.2005 · Cited by 78 · see citing works
Rzychon, M., Sabat, A. J., Kosowska, K., Potempa, J., & Dubin, A. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03613.x · Cited by 70 · see citing works
Thomsen, L. E., Olsen, J. E., Foster, J. W., & Ingmer, H. (2002) · Microbiology · doi:10.1099/00221287-148-9-2727 · Cited by 69 · see citing works
Self-citationPurdy, G. E., Hong, M., & Payne, S. M. (2002) · Infection and Immunity · doi:10.1128/iai.70.11.6355-6364.2002 · Cited by 68 · see citing works
Matsui, H., Suzuki, M., Isshiki, Y., Kodama, C., Eguchi, M., Kikuchi, Y., Motokawa, K., Takaya, A., Tomoyasu, T., & Yamamoto, T. (2002) · Infection and Immunity · doi:10.1128/iai.71.1.30-39.2003 · Cited by 67 · see citing works
Rigoulay, C., Entenza, J. M., Halpern, D., Widmer, E., Moreillon, P., Poquet, I., & Gruss, A. (2004) · Infection and Immunity · doi:10.1128/iai.73.1.563-572.2005 · Cited by 66 · see citing works
Smagur, J., Guzik, K., Magiera, Ł., Bzowska, M., Gruca, M., Thøgersen, I. B., Enghild, J. J., & Potempa, J. (2008) · Journal of Innate Immunity · doi:10.1159/000181014 · Cited by 64 · see citing works
Negative Regulation of Quorum-Sensing Systems inPseudomonas aeruginosaby ATP-Dependent Lon Protease
Takaya, A., Tabuchi, F., Tsuchiya, H., Isogai, E., & Yamamoto, T. (2008) · Journal of Bacteriology · doi:10.1128/jb.01873-07 · Cited by 64 · see citing works
Galvan, E. M., Lasaro, M. A., & Schifferli, D. M. (2008) · Infection and Immunity · doi:10.1128/iai.01197-07 · Cited by 64 · see citing works
Staphylococcus aureus -Derived Staphopain B, a Potent Cysteine Protease Activator of Plasma Chemerin
Kulig, P., Zabel, B. A., Dubin, G., Allen, S. J., Ohyama, T., Potempa, J., Handel, T. M., Butcher, E. C., & Cichy, J. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.6.3713 · Cited by 63 · see citing works
Yamamoto, T., Hanawa, T., Ogata, S., & Kamiya, S. (1996) · Infection and Immunity · doi:10.1128/iai.64.8.2980-2987.1996 · Cited by 63 · see citing works
Streptococcus pneumoniae: proteomics of surface proteins for vaccine development
Morsczeck, C. O., Prokhorova, T. A., Sigh, J., Pfeiffer, M., Bille-Nielsen, M., Petersen, J., Boysen, A., Kofoed, T., Møller, J. K., Nyborg-Nielsen, P., et al. (2007) · Clinical Microbiology and Infection · doi:10.1111/j.1469-0691.2007.01878.x · Cited by 63 · see citing works
Vogt, S. L., Nevesinjac, A. Z., Humphries, R. M., Donnenberg, M. S., Armstrong, G. D., & Raivio, T. L. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07145.x · Cited by 63 · see citing works
The chlamydial periplasmic stress response serine protease cHtrA is secreted into host cell cytosol
Wu, X. Y., Lei, L., Gong, S., Chen, D., Flores, R., & Zhong, G. (2011) · BMC Microbiology · doi:10.1186/1471-2180-11-87 · Cited by 62 · see citing works
Leduc, D., Beaufort, N., de Bentzmann, S., Rousselle, J.-C., Namane, A., Chignard, M., & Pidard, D. (2007) · Infection and Immunity · doi:10.1128/iai.00015-07 · Cited by 62 · see citing works
Regulated Proteolysis in Microorganisms
Dougan, D. A. (2013) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5940-4 · Cited by 61 · see citing works
Kage, H., Takaya, A., Ohya, M., & Yamamoto, T. (2008) · Journal of Bacteriology · doi:10.1128/jb.01385-07 · Cited by 60 · see citing works
Bæk, K. T., Vegge, C. S., Skórko‐Glonek, J., & Brøndsted, L. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.01603-10 · Cited by 58 · see citing works
Self-citationGaillot, O., Bregenholt, S., Jaubert, F., Santo, J. P. D., & Berche, P. (2001) · Infection and Immunity · doi:10.1128/iai.69.8.4938-4943.2001 · Cited by 58 · see citing works
Haiko, J., Laakkonen, L. J., Juuti, K. M., Kalkkinen, N., & Korhonen, T. (2010) · Journal of Bacteriology · doi:10.1128/jb.00458-10 · Cited by 56 · see citing works
Borezée, E., Pellegrini, E., Béretti, J., & Berche, P. (2001) · Microbiology · doi:10.1099/00221287-147-11-2913 · Cited by 55 · see citing works
Streptococcus agalactiae CspA Is a Serine Protease That Inactivates Chemokines
Bryan, J. D., & Shelver, D. W. (2008) · Journal of Bacteriology · doi:10.1128/jb.01124-08 · Cited by 55 · see citing works
Lewis, C., Skovierova, H., Rowley, G., Rezuchova, B., Homerova, D., Stevenson, A., Spencer, J., Farn, J., Kormanec, J., & Roberts, M. (2009) · Microbiology · doi:10.1099/mic.0.023754-0 · Cited by 54 · see citing works
HtrA is a major virulence determinant of Bacillus anthracis
Chitlaru, T., Zaide, G., Ehrlich, S., Inbar, I., Cohen, O., & Avigdor Shafferman, C. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07790.x · Cited by 54 · see citing works
HtrA chaperone activity contributes to host cell binding in Campylobacter jejuni
Bæk, K. T., Vegge, C. S., & Brøndsted, L. (2011) · Gut Pathogens · doi:10.1186/1757-4749-3-13 · Cited by 53 · see citing works
Self-citationNickerson, N. N., Joag, V., & Mcgavin, M. J. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06384.x · Cited by 50 · see citing works
Wu, K., Zhang, X., Shi, J., Li, N., Li, D., Luo, M., Cao, J., Yin, N., Wang, H., Xu, W., et al. (2009) · Infection and Immunity · doi:10.1128/iai.00473-09 · Cited by 49 · see citing works
Role of group A Streptococcus HtrA in the maturation of SpeB protease
Cole, J. N., Aquilina, J. A., Hains, P. G., Henningham, A., Sriprakash, K. S., Caparon, M. G., Nizet, V., Kotb, M., Cordwell, S. J., Djordjevic, S. P., et al. (2007) · PROTEOMICS · doi:10.1002/pmic.200700626 · Cited by 48 · see citing works
Role of DegP for two‐partner secretion in Bordetella
Baud, C., Hodak, H., Willery, E., Drobecq, H., Locht, C., Jamin, M., & Jacob‐Dubuisson, F. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06860.x · Cited by 47 · see citing works
Jelsbak, L., Ingmer, H., Valihrach, L., Cohn, M. T., Christiansen, M. H. G., Kallipolitis, B. H., & Frees, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012752 · Cited by 44 · see citing works
Self-citationNickerson, N. N., Ip, J., Passos, D. T., & Mcgavin, M. J. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06974.x · Cited by 42 · see citing works
Acyl depsipeptide (ADEP) resistance in Streptomyces
Gominet, M., Seghezzi, N., & Mazodier, P. (2011) · Microbiology · doi:10.1099/mic.0.048454-0 · Cited by 39 · see citing works
Ramu, P., Lobo, L. A., Kukkonen, M., Bjur, E., Suomalainen, M., Raukola, H., Miettinen, M., Julkunen, I., Holst, O., Rhen, M., et al. (2007) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2007.06.004 · Cited by 35 · see citing works
Humphries, R. M., Griener, T. P., Vogt, S. L., Mulvey, G. L., Raivio, T. L., Donnenberg, M. S., Kitov, P. I., Surette, M. G., & Armstrong, G. D. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07192.x · Cited by 33 · see citing works
Proteolytic Regulation of Stress Response Pathways in Escherichia coli
Micevski, D., & Dougan, D. A. (2013) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5940-4_5 · Cited by 31 · see citing works
YidC Is Involved in the Biogenesis of the Secreted Autotransporter Hemoglobin Protease
Jong, W. S. P., ten Hagen‐Jongman, C. M., Ruijter, E., Orrù, R. V. A., Genevaux, P., & Luirink, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.167650 · Cited by 31 · see citing works
Bertani, I., Rampioni, G., Leoni, L., & Venturi, V. (2007) · BMC Microbiology · doi:10.1186/1471-2180-7-71 · Cited by 30 · see citing works
Activation of human pro-urokinase by unrelated proteases secreted by Pseudomonas aeruginosa
Beaufort, N., Seweryn, P., de Bentzmann, S., Tang, A., Kellermann, J., Grebenchtchikov, N. I., Schmitt, M., Sommerhoff, C. P., Pidard, D., & Magdolen, V. (2010) · Biochemical Journal · doi:10.1042/bj20091806 · Cited by 22 · see citing works
Cao, J., Li, D., Gong, Y., Yin, N., Chen, T., Wong, C. K., Xu, W., Luo, J., Zhang, X., Lam, C. W. K., et al. (2009) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2008.03866.x · Cited by 19 · see citing works
Membrane‐associated DegP in Bordetella chaperones a repeat‐rich secretory protein
Baud, C., Gutsche, I., Willery, E., Paepe, D. C., Drobecq, H., Gilleron, M., Locht, C., Jamin, M., & Jacob‐Dubuisson, F. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07672.x · Cited by 17 · see citing works
Assemblies of DegP underlie its dual chaperone and protease function
Subrini, O., & Betton, J. (2009) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2009.01658.x · Cited by 16 · see citing works
Šplı́chal, I., Rychlı́k, I., Gregorová, D., Šebková, A., Trebichavský, I., Šplı́chalová, A., Muneta, Y., & Mori, Y. (2007) · Immunobiology · doi:10.1016/j.imbio.2007.05.001 · Cited by 6 · see citing works
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Helicobacter pylori Virulence Factors Exploiting Gastric Colonization and its Pathogenicity
Ansari, S., & Yamaoka, Y. (2019) · Toxins · doi:10.3390/toxins11110677 · Cited by 295 · see citing works
Helicobacter pylori: an up-to-date overview on the virulence and pathogenesis mechanisms
Sharndama, H. C., & Mba, I. E. (2022) · Brazilian Journal of Microbiology · doi:10.1007/s42770-021-00675-0 · Cited by 266 · see citing works
Proteases and protease inhibitors in infectious diseases
Agbowuro, A. A., Huston, W. M., Gamble, A. B., & Tyndall, J. D. A. (2017) · Medicinal Research Reviews · doi:10.1002/med.21475 · Cited by 188 · see citing works
Remote near infrared identification of pathogens with multiplexed nanosensors
Nißler, R., Bader, O., Dohmen, M., Walter, S. G., Noll, C., Selvaggio, G., Groß, U., & Kruss, S. (2020) · Nature Communications · doi:10.1038/s41467-020-19718-5 · Cited by 179 · see citing works
Frees, D., Gerth, U., & Ingmer, H. (2013) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2013.11.009 · Cited by 172 · see citing works
Self-citationProtease-activated receptors (PARs)—biology and role in cancer invasion and metastasis
Wojtukiewicz, M. Z., Hempel, D., Sierko, E., Tucker, S. C., & Honn, K. V. (2015) · Cancer and Metastasis Reviews · doi:10.1007/s10555-015-9599-4 · Cited by 147 · see citing works
Extracellular HtrA serine proteases: An emerging new strategy in bacterial pathogenesis
Backert, S., Bernegger, S., Skórko‐Glonek, J., & Weßler, S. (2018) · Cellular Microbiology · doi:10.1111/cmi.12845 · Cited by 133 · see citing works
Bæk, K. T., Gründling, A., Mogensen, R. G., Thøgersen, L., Petersen, A., Paulander, W., & Frees, D. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02802-14 · Cited by 107 · see citing works
Self-citationRamírez-Larrota, J. S., & Eckhard, U. (2022) · Biomolecules · doi:10.3390/biom12020306 · Cited by 108 · see citing works
The architecture of neutrophil extracellular traps investigated by atomic force microscopy
Pires, R. H., Felix, S. B., & Delcea, M. (2016) · Nanoscale · doi:10.1039/c6nr03416k · Cited by 94 · see citing works
The emerging roles of bacterial proteases in intestinal diseases
Caminero, A., Guzman, M., Libertucci, J., & Lomax, A. E. (2023) · Gut Microbes · doi:10.1080/19490976.2023.2181922 · Cited by 92 · see citing works
Heimesaat, M. M., Alutis, M. E., Grundmann, U., Fischer, A., Tegtmeyer, N., Böhm, M., Kühl, A. A., Göbel, U. B., Backert, S., & Bereswill, S. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00077 · Cited by 92 · see citing works
Location-specific signatures of Crohn’s disease at a multi-omics scale
Gonzalez, C. G., Mills, R. H., Zhu, Q., Sauceda, C., Knight, R. D., Dulai, P. S., & Gonzalez, D. J. (2022) · Microbiome · doi:10.1186/s40168-022-01331-x · Cited by 90 · see citing works
Pachathundikandi, S. K., Tegtmeyer, N., & Backert, S. (2013) · Gut Microbes · doi:10.4161/gmic.27001 · Cited by 83 · see citing works
Tegtmeyer, N., Moodley, Y., Yamaoka, Y., Pernitzsch, S. R., Schmidt, V., Rivas-Traverso, F., Schmidt, T. P., Rad, R., Yeoh, K. G., Ho, B., et al. (2015) · Molecular Microbiology · doi:10.1111/mmi.13276 · Cited by 78 · see citing works
An innovative approach of bioremediation in enzymatic degradation of xenobiotics
Rathore, S., Varshney, A., Mohan, S., & Dahiya, P. (2022) · Biotechnology and Genetic Engineering Reviews · doi:10.1080/02648725.2022.2027628 · Cited by 75 · see citing works
Boehm, M., Lind, J., Backert, S., & Tegtmeyer, N. (2015) · European Journal of Microbiology and Immunology · doi:10.1556/eujmi-d-15-00003 · Cited by 62 · see citing works
Gur, E. (2013) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5940-4_2 · Cited by 62 · see citing works
Cellular functions of the ClpP protease impacting bacterial virulence
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Runde, S., Molière, N., Heinz, A., Maisonneuve, E., Janczikowski, A., Elsholz, A. K. W., Gerth, U., Hecker, M., & Turgay, K. (2014) · Molecular Microbiology · doi:10.1111/mmi.12521 · Cited by 61 · see citing works
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Dawoud, T. M. S., Davis, M. L., Park, S. H., Kim, S. A., Kwon, Y. M., Jarvis, N. A., O’Bryan, C. A., Shi, Z., Crandall, P. G., & Ricke, S. C. (2017) · Frontiers in Veterinary Science · doi:10.3389/fvets.2017.00093 · Cited by 56 · see citing works
Zarzecka, U., Modrak‐Wójcik, A., Figaj, D., Apanowicz, M., Lesner, A., Bzowska, A., Lipińska, B., Zawilak-Pawlik, A. M., Backert, S., & Skórko‐Glonek, J. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00961 · Cited by 56 · see citing works
Beshiru, A., Igbinosa, I. H., & Igbinosa, E. O. (2018) · PLoS ONE · doi:10.1371/journal.pone.0204345 · Cited by 52 · see citing works
Bacterial serine protease HtrA as a promising new target for antimicrobial therapy?
Weßler, S., Schneider, G., & Backert, S. (2017) · Cell Communication and Signaling · doi:10.1186/s12964-017-0162-5 · Cited by 50 · see citing works
Harrer, A., Boehm, M., Backert, S., & Tegtmeyer, N. (2017) · Gut Pathogens · doi:10.1186/s13099-017-0189-6 · Cited by 50 · see citing works
Abfalter, C. M., Schubert, M., Goetz, C., Schmidt, T. P., Posselt, G., & Weßler, S. (2016) · Cell Communication and Signaling · doi:10.1186/s12964-016-0153-y · Cited by 48 · see citing works
Stelzner, K., Boyny, A., Hertlein, T., Sroka, A., Moldovan, A., Paprotka, K., Kessie, D. K., Mehling, H., Potempa, J., Ohlsen, K., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009874 · Cited by 51 · see citing works
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Beshiru, A., & Igbinosa, E. O. (2018) · Microbial Pathogenesis · doi:10.1016/j.micpath.2018.04.015 · Cited by 45 · see citing works
Function of serine protease HtrA in the lifecycle of the foodborne pathogen Campylobacter jejuni
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Zhang, Q., & Zhang, C. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.0c04538 · Cited by 41 · see citing works
Ye, M., Sharma, K., Thakur, M., Smith, A. A., Büyüktanır, Ö., Xiang, X., Yang, X., Promnares, K., Lou, Y., Yang, X. F., et al. (2016) · Infection and Immunity · doi:10.1128/iai.00360-16 · Cited by 41 · see citing works
Molecular and pathogenic characterization of Vibrio parahaemolyticus isolated from seafood
Ashrafudoulla, M., Na, K. W., Hossain, M. I., Mizan, M. F. R., Nahar, S., Toushik, S. H., Roy, P. K., Park, S. H., & Ha, S. (2021) · Marine Pollution Bulletin · doi:10.1016/j.marpolbul.2021.112927 · Cited by 40 · see citing works
Siddique, A., Azim, S., Ali, A., Andleeb, S., Ahsan, A., Imran, M., & Rahman, A. (2021) · Antibiotics · doi:10.3390/antibiotics10070785 · Cited by 39 · see citing works
Mazzei, R., Leonti, M., Spadafora, S., Patitucci, A., & Tagarelli, G. (2019) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2019.112443 · Cited by 37 · see citing works
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Machuca, Á., & Martinez, V. (2016) · PLoS ONE · doi:10.1371/journal.pone.0168855 · Cited by 34 · see citing works
Bernegger, S., Brunner, C., Vizovišek, M., Fonovič, M., Cuciniello, G., Giordano, F., Stanojlović, V., Jarząb, M., Simister, P. C., Feller, S. M., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-67578-2 · Cited by 32 · see citing works
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Albrecht, N., Tegtmeyer, N., Sticht, H., Skórko‐Glonek, J., & Backert, S. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00642 · Cited by 30 · see citing works
Global proteomic profiling of Yersinia ruckeri strains
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Lelis, T., Peng, J., Barphagha, I., Chen, R., & Ham, J. H. (2019) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-11-18-0312-r · Cited by 29 · see citing works
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Tapader, R., Basu, S., & Pal, A. (2019) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2019.03.002 · Cited by 28 · see citing works
Singh, S., Mallik, S. K., Kala, K., Shahi, N., Pathak, R., Giri, A. K., Chandra, S., Pant, K., & Patiyal, R. S. (2021) · Aquaculture · doi:10.1016/j.aquaculture.2021.737118 · Cited by 28 · see citing works
Boehm, M., Haenel, I., Hoy, B., Brøndsted, L., Smith, T. G., Hoover, T. R., Weßler, S., & Tegtmeyer, N. (2013) · European Journal of Microbiology and Immunology · doi:10.1556/eujmi.3.2013.3.3 · Cited by 28 · see citing works
Self-citationAbfalter, C. M., Schönauer, E., Ponnuraj, K., Huemer, M., Gadermaier, G., Regl, C., Briza, P., Ferreira, F., Huber, C. G., Brandstetter, H., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0162433 · Cited by 28 · see citing works
Ciastoń, I., Dobosz, E., Potempa, J., & Kozieł, J. (2022) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2022.101143 · Cited by 27 · see citing works
A, M. R. P. (2014) · Enzyme Engineering · doi:10.4172/2329-6674.1000126 · Cited by 26 · see citing works
Kikuchi, T., Dayı, M., Hunt, V. L., Ishiwata, K., Toyoda, A., Kounosu, A., Sun, S., Maeda, Y., Kondo, Y., de Noya, B. A., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02160-8 · Cited by 24 · see citing works
The LA Loop as an Important Regulatory Element of the HtrA (DegP) Protease from Escherichia coli
Figaj, D., Giełdoń, A., Polit, A., Sobiecka-Szkatuła, A., Koper, T., Denkiewicz-Kruk, M., Banecki, B., Lesner, A., Ciarkowski, J., Lipińska, B., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.532895 · Cited by 24 · see citing works
Otigbu, A. C., Clarke, A. M., Fri, J., Akanbi, O. E., & Njom, H. A. (2018) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph15050925 · Cited by 24 · see citing works
Zhang, Z., Huang, Q., Tao, X., Song, G., Zheng, P., Li, H., Sun, H., & Xia, W. T. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007387 · Cited by 24 · see citing works
Saldarriaga‐Córdoba, M., Irgang, R., & Avendaño-Herrera, R. E. (2021) · Journal of Fish Diseases · doi:10.1111/jfd.13503 · Cited by 23 · see citing works
Camberlein, V., Jézéquel, G., Haupenthal, J., & Hirsch, A. K. H. (2022) · Antibiotics · doi:10.3390/antibiotics11081060 · Cited by 23 · see citing works
Poyatos‐Racionero, E., Borràs, G. G., Ruiz‐Rico, M., Morellá‐Aucejo, Á., Aznar, E., Baviera, J. M. B., Martínez‐Máñez, R., Marcos, M. D., & Bernardos, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073795 · Cited by 22 · see citing works
Harkness, R. W., Toyama, Y., Ripstein, Z. A., Zhao, H.-Y., Sever, A. I. M., Luan, Q., Brady, J. P., Clark, P. L., Schuck, P., & Kay, L. (2021) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2109732118 · Cited by 19 · see citing works
Renoz, F., Champagne, A., Degand, H., Faber, A., Morsomme, P., Foray, V., & Hance, T. (2017) · PeerJ · doi:10.7717/peerj.3291 · Cited by 20 · see citing works
Huang, H.-H., Lin, Y.-T., Chen, P.-Y., Li, L.-H., Ning, H., & Yang, T. (2018) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00554-18 · Cited by 22 · see citing works
Remodeling of the Streptococcus mutans proteome in response to LrgAB and external stresses
Ahn, S., Gu, T., Koh, J., & Rice, K. C. (2017) · Scientific Reports · doi:10.1038/s41598-017-14324-w · Cited by 21 · see citing works
Lu, H.-F., Wu, B.-K., Huang, Y.-W., LEE, M.-Z., Li, M.-F., Ho, H.-J., Yang, H.-C., & Yang, T. (2020) · BMC Microbiology · doi:10.1186/s12866-020-01989-z · Cited by 20 · see citing works
Sharafutdinov, I., Tegtmeyer, N., Rohde, M., Olofsson, A., Rehman, Z. U., Arnqvist, A., & Backert, S. (2024) · Cells · doi:10.3390/cells13030224 · Cited by 20 · see citing works
Figaj, D., Czaplewska, P., Przepióra, T., Ambroziak, P., Potrykus, M., & Skórko‐Glonek, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103687 · Cited by 19 · see citing works
Mellergaard, M., Høgh, R. I., Lund, A., Aldana, B. I., Guérillot, R., Møller, S. H., Hayes, A. S., Panagiotopoulou, N., Frimand, Z., Jepsen, S. D., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012673 · Cited by 19 · see citing works
Self-citationVieira, P. C., Espinoza-Culupú, A. O., Nepomuceno, R. S. L., Alves, M. R., Lebrun, I., Elias, W. P., & Ruiz, R. C. (2020) · PLoS ONE · doi:10.1371/journal.pone.0228959 · Cited by 19 · see citing works
Tsaplina, O. A., Demidyuk, I. V., Artamonova, T., Khodorkovsky, M., & Khaitlina, S. Y. (2020) · FEBS Letters · doi:10.1002/1873-3468.13897 · Cited by 19 · see citing works
Synthesis and Antichlamydial Activity of Molecules Based on Dysregulators of Cylindrical Proteases
Seleem, M. A., de Almeida, N. R., Chhonker, Y. S., Murry, D. J., Guterres, Z. D. R., Blocker, A. M., Kuwabara, S., Fisher, D. J., Leal, E. S., Martinefski, M., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00371 · Cited by 18 · see citing works
Corrêa, A. F., Bastos, I. M. D., Neves, D., Kipnis, A., Junqueira‐Kipnis, A. P., & Santana, J. M. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00504 · Cited by 18 · see citing works
Vida, C., Cazorla, F. M., & de Vicente, A. (2017) · Research in Microbiology · doi:10.1016/j.resmic.2017.03.007 · Cited by 17 · see citing works
Evolution and Role of Proteases in Campylobacter jejuni Lifestyle and Pathogenesis
Linz, B., Sharafutdinov, I., Tegtmeyer, N., & Backert, S. (2023) · Biomolecules · doi:10.3390/biom13020323 · Cited by 16 · see citing works
Extracellular Pneumococcal Serine Proteases Affect Nasopharyngeal Colonization
Ali, M. Q., Kohler, T. P., Burchhardt, G., Wüst, A., Henck, N., Bolsmann, R., Voß, F., & Hammerschmidt, S. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.613467 · Cited by 16 · see citing works
Flexible Client-Dependent Cages in the Assembly Landscape of the Periplasmic Protease-Chaperone DegP
Harkness, R. W., V, Ripstein, Z. A., Trani, J. M. D., & Kay, L. E. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c11849 · Cited by 15 · see citing works
Biochemical properties of the HtrA homolog from bacterium Stenotrophomonas maltophilia
Zarzecka, U., Modrak‐Wójcik, A., Bayassi-Jakowicka, M., Szewczyk, M., Giełdoń, A., Lesner, A., Koper, T., Bzowska, A., Sanguinetti, M., Backert, S., et al. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.11.086 · Cited by 14 · see citing works
Bai, M., Dai, J., Hu, W., Li, C., Cui, H., & Lin, L. (2023) · Food Bioscience · doi:10.1016/j.fbio.2023.103137 · Cited by 13 · see citing works
ClpP Peptidase as a Plausible Target for the Discovery of Novel Antibiotics
Bhardwaj, S., & Roy, K. K. (2023) · Current Drug Targets · doi:10.2174/0113894501274958231220053714 · Cited by 13 · see citing works
Taste shaped the use of botanical drugs
Leonti, M., Baker, J., Staub, P. O., Casu, L., & Hawkins, J. A. (2023) · eLife · doi:10.7554/elife.90070 · Cited by 12 · see citing works
Ge, Z., Yuan, P., Chen, L., Chen, J., Shen, D., She, Z., & Lu, Y. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100233 · Cited by 12 · see citing works
Environmental factors drive bacterial degradation of gastrointestinal mucus
Arias, S. L., van Wijngaarden, E. W., Balint, D., Jones, J. P., Crawford, C. C., Shukla, P. J., Silberstein, M. N., & Brito, I. (2025) · npj Biofilms and Microbiomes · doi:10.1038/s41522-025-00741-7 · Cited by 12 · see citing works
Koper, T., Polit, A., Sobiecka-Szkatuła, A., Wegrzyn, K. E., Scirè, A., Figaj, D., Kadziński, L., Zarzecka, U., Żurawa‐Janicka, D., Banecki, B., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0117413 · Cited by 11 · see citing works
Mallik, S. K., Pathak, R., Shahi, N., Kala, K., Chandra, S., Das, P., Singh, B., Singh, M., Giri, A. K., Tandel, R. S., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-40028-5 · Cited by 10 · see citing works
Abfalter, C. M., Schmidt, T. P., & Weßler, S. (2015) · British Microbiology Research Journal · doi:10.9734/bmrj/2015/16402 · Cited by 10 · see citing works
Lee, J. H., & Zhao, Y. F. (2017) · Phytopathology · doi:10.1094/phyto-06-17-0198-r · Cited by 10 · see citing works
Hickey, M. E., Accumanno, G. M., McIntosh, D., Blank, G. S., & Lee, J. (2014) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.6784 · Cited by 10 · see citing works
Deconvolving multiplexed protease signatures with substrate reduction and activity clustering
Zhuang, Q. K.-W., Holt, B. A., Kwong, G. A., & Qiu, P. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006909 · Cited by 9 · see citing works
Figueroa, J. E., Villagrán, D., Cartes, C., Solís, C. J., Nourdin, G., & Haussmann, D. (2021) · Journal of Fish Diseases · doi:10.1111/jfd.13333 · Cited by 9 · see citing works
Kotb, E., El-Zawahry, Y. A., & Saleh, G. E. (2019) · Journal of Biosciences · doi:10.1007/s12038-018-9829-3 · Cited by 8 · see citing works
Rodrigues, J. F., Lourenço, R. F., Maeda, D. L. N. F., Cintra, M. D. J., Nakao, N., Mathias-Santos, C., Luiz, W. B., & Ferreira, L. C. D. S. (2020) · Brazilian Journal of Microbiology · doi:10.1007/s42770-020-00231-2 · Cited by 8 · see citing works
Wang, Y., Jiang, N., Wang, B., Tao, H., Zhang, X., Guan, Q., & Liu, C. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.590851 · Cited by 8 · see citing works
Mu, S., Sun, J., Gao, L., Li, Y., Wang, Z., Chang, R., Jiang, J., Wang, L., Wang, L., & Song, L. (2025) · Microbiology Spectrum · doi:10.1128/spectrum.00173-25 · Cited by 6 · see citing works
Targeting Quorum Sensing Mediated Staphylococcus aureus Biofilms: A Proteolytic Approach
Kalia, V. C., Koul, S., Ray, S., & Prakash, J. (2018) · Springer eBooks · doi:10.1007/978-981-10-9026-4_2 · Cited by 6 · see citing works
Harkness, R. W., V, Zhao, H., Toyama, Y., Schuck, P., & Kay, L. E. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c13247 · Cited by 6 · see citing works
Leoni, E. (2019) · MDPI eBooks · doi:10.3390/books978-3-03897-579-3 · Cited by 6 · see citing works
Satała, D., Satała, G., Kulig, K., Karkowska‐Kuleta, J., Kozik, A., & Rąpała‐Kozik, M. (2025) · Scientific Reports · doi:10.1038/s41598-025-15577-6 · Cited by 5 · see citing works
Secretome analysis and virulence assessment in Abiotrophia defectiva
Bhardwaj, R. G., Khalaf, M. E., & Karched, M. (2024) · Journal of Oral Microbiology · doi:10.1080/20002297.2024.2307067 · Cited by 5 · see citing works
Kodous, A. S., Fathy, R. M., Mazhar, A., Shafaa, M. W., & Shalaby, M. S. (2025) · Process Biochemistry · doi:10.1016/j.procbio.2025.03.009 · Cited by 5 · see citing works
Daroz, B. B., Fernandes, L. G. V., Teixeira, A. F., & Nascimento, A. L. T. O. (2020) · Tropical Medicine and Infectious Disease · doi:10.3390/tropicalmed5040179 · Cited by 5 · see citing works
Degron-mediated proteolysis of CrhR-like DEAD-box RNA helicases in cyanobacteria
Whitman, B. T., Murray, C., Whitford, D. S., Paul, S. S., Fahlman, R. P., Glover, M. J. N., & Owttrim, G. W. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101925 · Cited by 4 · see citing works
Jeong, B., Jang, H. A., Lee, J., Bae, H. R., & Kim, J. K. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.04330-22 · Cited by 4 · see citing works
The key to unlock the Hsp 100/ Clp protein degradation machines of M ycobacterium
Molière, N., & Turgay, K. (2014) · Molecular Microbiology · doi:10.1111/mmi.12696 · Cited by 3 · see citing works
Zhang, W., Yan, H., Zhu, Z., Zhang, C., Du, P., Zhao, W., & Li, W. (2020) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2000281 · Cited by 3 · see citing works
- Authors
- Frees, D., Brøndsted, L., & Ingmer, H.
- Affiliations
- University of Copenhagen (DK)
- Corresponding author
- Ingmer, Hanne
- Venue
- Subcellular Biochemistry
- Publisher
- Springer Netherlands
- Published
- 2013
- Volume
- 66
- Pages
- 161-192
- ISSN
- 0306-0225 (ISSN-L)
- OpenAlex
- W155982093
- Cited by
- 159
- References
- 146
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 5 · 2023: 15 · 2022: 11 · 2021: 12 · 2020: 37 · 2019: 13 · 2018: 11 · 2017: 15 · 2016: 6 · 2015: 7 · 2014: 7 · 2013: 6
- FWCI
- 22.02
- Type
- book chapter
- Language
- en
- Open access
- closed
- Licence
- Locations
- Sub-cellular biochemistry/Subcellular biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- bacterial proteases, bacterial virulence, Clp protease, Lon protease, HtrA protease, extracellular protease, stress tolerance, substrate specificity, chaperone activity, zymogen activation, proteolytic maturation, host cell signalling, bacterial pathogenesis
- MeSH terms
- Bacteria, Bacterial Proteins, Humans, Peptide Hydrolases, Virulence, Signal Transduction, Molecular Chaperones, Proteolysis
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